H-Lys(Abz)-Pro-Pro-pNA

Description:

Internally quenched fluorogenic (FRET) substrate which allows aminopeptidase P (APP) activity determination by a continuous fluorescent assay.

Sequence:

K(Abz)PP-p-Nitroanilide

General

References

Comments (0)

Name	H-Lys(Abz)-Pro-Pro-pNA
Category	Enzyme Substrates and Inhibitors
One Letter Code	K(Abz)PP-p-Nitroanilide
Three Letter Code	{Lys(Abz)}{Pro}{Pro}-p-Nitroanilide
Molecular Weight	579.660
Application

Poras, Hervé, et al. "A sensitive fluorigenic substrate for selective in vitro and in vivo assay of leukotriene A4 hydrolase activity." Analytical biochemistry 441.2 (2013): 152-161.

Abid, Karim, et al. "Kinetic study of neuropeptide Y (NPY) proteolysis in blood and identification of NPY3–35 a new peptide generated by plasma kallikrein." Journal of Biological Chemistry 284.37 (2009): 24715-24724.

Dalal, Seema, and Michael Klemba. "Roles for two aminopeptidases in vacuolar hemoglobin catabolism in Plasmodium falciparum." Journal of Biological Chemistry 282.49 (2007): 35978-35987.

Graham, Stephen C., et al. "Kinetic and crystallographic analysis of mutant Escherichia coli aminopeptidase P: insights into substrate recognition and the mechanism of catalysis." Biochemistry 45.3 (2006): 964-975.

Brandt, I., J. Joossens, and X. Chen. "Inhibition of dipeptidyl-peptidase IV catalyzed peptide truncation by vildagliptin ((2S)-{acetyl}-pyrrolidine-2-carbonitrile)." Biochem Pharmacol 70 (2005): 134.

Monod, Michel, et al. "Aminopeptidases and dipeptidyl-peptidases secreted by the dermatophyte Trichophyton rubrum." Microbiology 151.1 (2005): 145-155.